eF-site ID 2oag-AB
PDB Code 2oag
Chain A, B

click to enlarge
Title Crystal structure of human dipeptidyl peptidase IV (DPPIV) with pyrrolidine-constrained phenethylamine 29g
Classification HYDROLASE/HYDROLASE INHIBITOR
Compound Dipeptidyl peptidase 4
Source null (DPP4_HUMAN)
Sequence A:  SRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV
FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY
NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS
PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI
TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY
SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS
VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR
IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR
PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT
KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD
YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP
LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII
LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV
FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL
GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM
VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED
NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ
ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF
IKQCFS
B:  SRKTYTLTDYLKNTYRLKLYSLRWISDHEYLYKQENNILV
FNAEYGNSSVFLENSTFDEFGHSINDYSISPDGQFILLEY
NYVKQWRHSYTASYDIYDLNKRQLITEERIPNNTQWVTWS
PVGHKLAYVWNNDIYVKIEPNLPSYRITWTGKEDIIYNGI
TDWVYEEEVFSAYSALWWSPNGTFLAYAQFNDTEVPLIEY
SFYSDESLQYPKTVRVPYPKAGAVNPTVKFFVVNTDSLSS
VTNATSIQITAPASMLIGDHYLCDVTWATQERISLQWLRR
IQNYSVMDICDYDESSGRWNCLVARQHIEMSTTGWVGRFR
PSEPHFTLDGNSFYKIISNEEGYRHICYFQIDKKDCTFIT
KGTWEVIGIEALTSDYLYYISNEYKGMPGGRNLYKIQLSD
YTKVTCLSCELNPERCQYYSVSFSKEAKYYQLRCSGPGLP
LYTLHSSVNDKGLRVLEDNSALDKMLQNVQMPSKKLDFII
LNETKFWYQMILPPHFDKSKKYPLLLDVYAGPCSQKADTV
FRLNWATYLASTENIIVASFDGRGSGYQGDKIMHAINRRL
GTFEVEDQIEAARQFSKMGFVDNKRIAIWGWSYGGYVTSM
VLGSGSGVFKCGIAVAPVSRWEYYDSVYTERYMGLPTPED
NLDHYRNSTVMSRAENFKQVEYLLIHGTADDNVHFQQSAQ
ISKALVDVGVDFQAMWYTDEDHGIASSTAHQHIYTHMSHF
IKQCFS
Description


Functional site
1) chain B
residue 125
type
sequence R
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
2) chain B
residue 205
type
sequence E
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
3) chain B
residue 206
type
sequence E
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
4) chain B
residue 207
type
sequence V
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
5) chain B
residue 209
type
sequence S
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
6) chain B
residue 357
type
sequence F
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
7) chain B
residue 358
type
sequence R
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
8) chain B
residue 547
type
sequence Y
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
9) chain B
residue 630
type
sequence S
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
10) chain B
residue 631
type
sequence Y
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
11) chain B
residue 656
type
sequence V
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
12) chain B
residue 662
type
sequence Y
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
13) chain B
residue 666
type
sequence Y
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
14) chain B
residue 710
type
sequence N
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
15) chain B
residue 711
type
sequence V
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
16) chain B
residue 740
type
sequence H
description BINDING SITE FOR RESIDUE DLI B 4000
source : AC1
17) chain A
residue 92
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI3
18) chain B
residue 92
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI3
19) chain A
residue 150
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI4
20) chain B
residue 150
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI4
21) chain A
residue 219
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI5
22) chain B
residue 219
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI5
23) chain A
residue 281
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI6
24) chain B
residue 281
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI6
25) chain A
residue 321
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI7
26) chain B
residue 321
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI7
27) chain A
residue 520
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI8
28) chain B
residue 520
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI8
29) chain A
residue 685
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
source Swiss-Prot : SWS_FT_FI9
30) chain B
residue 685
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218
source Swiss-Prot : SWS_FT_FI9
31) chain B
residue 630
type ACT_SITE
sequence S
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1
32) chain B
residue 708
type ACT_SITE
sequence D
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1
33) chain B
residue 740
type ACT_SITE
sequence H
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1
34) chain A
residue 630
type ACT_SITE
sequence S
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1
35) chain A
residue 708
type ACT_SITE
sequence D
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1
36) chain A
residue 740
type ACT_SITE
sequence H
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU10084
source Swiss-Prot : SWS_FT_FI1
37) chain A
residue 229
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2
38) chain B
residue 85
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2
39) chain B
residue 229
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2
40) chain A
residue 85
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:12483204, ECO:0000269|PubMed:12646248, ECO:0000269|PubMed:12906826, ECO:0000269|PubMed:20684603, ECO:0000269|PubMed:23835475, ECO:0007744|PDB:4L72
source Swiss-Prot : SWS_FT_FI2
41) chain A
residue 605-635
type prosite
sequence DQIEAARQFSKMGFVDNKRIAIWGWSYGGYV
description PRO_ENDOPEP_SER Prolyl endopeptidase family serine active site. DqieAarqFskmgfvdnkriaiwGwSyGGYV
source prosite : PS00708
42) chain A
residue 547
type catalytic
sequence Y
description 169
source MCSA : MCSA1
43) chain A
residue 630
type catalytic
sequence S
description 169
source MCSA : MCSA1
44) chain A
residue 631
type catalytic
sequence Y
description 169
source MCSA : MCSA1
45) chain A
residue 708
type catalytic
sequence D
description 169
source MCSA : MCSA1
46) chain A
residue 740
type catalytic
sequence H
description 169
source MCSA : MCSA1
47) chain B
residue 547
type catalytic
sequence Y
description 169
source MCSA : MCSA2
48) chain B
residue 630
type catalytic
sequence S
description 169
source MCSA : MCSA2
49) chain B
residue 631
type catalytic
sequence Y
description 169
source MCSA : MCSA2
50) chain B
residue 708
type catalytic
sequence D
description 169
source MCSA : MCSA2
51) chain B
residue 740
type catalytic
sequence H
description 169
source MCSA : MCSA2

Display surface

Download
Links